# STOCKHOLM 1.0 #=GF ID Bd3614-deam #=GF AC PF14439.1 #=GF DE Bd3614-like deaminase #=GF AU Iyer LM, Zhang D, Aravind L #=GF SE Manual #=GF GA 38.50 38.50; #=GF TC 39.20 130.90; #=GF NC 37.70 37.30; #=GF BM hmmbuild HMM.ann SEED.ann #=GF SM hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq #=GF TP Family #=GF RN [1] #=GF RM 21890906 #=GF RT Evolution of the deaminase fold and multiple origins of #=GF RT eukaryotic editing and mutagenic nucleic acid deaminases from #=GF RT bacterial toxin systems. #=GF RA Iyer LM, Zhang D, Rogozin IB, Aravind L; #=GF RL Nucleic Acids Res. 2011; [Epub ahead of print] #=GF DR INTERPRO; IPR025853; #=GF CC A member of the nucleic acid/nucleotide deaminase superfamily #=GF CC prototyped by Bdellovibrio Bd3614 [1]. They are typified by a #=GF CC distinct N-terminal globular domain. The Bdellovibrio version #=GF CC occurs in a predicted operon with a 23S rRNA G2445-modifying #=GF CC methylase suggesting that it might be involved in RNA editing #=GF CC [1]. #=GF SQ 4 #=GS A4S9Y1_OSTLU/127-236 AC A4S9Y1.1 #=GS C1MW10_MICPC/272-409 AC C1MW10.1 #=GS Q6MHD6_BDEBA/164-275 AC Q6MHD6.1 #=GS C1EBX0_MICSR/256-391 AC C1EBX0.1 A4S9Y1_OSTLU/127-236 RSRRGRDRKVFAALHSPTRGGVYAVAANTNGGNAVLHAEMNLLFPADDARA......................RRLIEPDTTLLVTLQCCRMCAARAVELGV.......RRAAYLREDPGPLASRTALAALARESRFDL C1MW10_MICPC/272-409 KARWRRDRRVVAMVVDRD.GVLVDAAVNTNAENAMLHAEFNLLMPWLMRLDGDGDGDGDGDGDGDGDGDGEAARKSLPPGARLFVSLQCCAMCAALVCAASDARGGEVLTDVVYGEEDPGALARDTELRRRGWERKRDE Q6MHD6_BDEBA/164-275 SVLHDYDRDIAAFLLNDQ.GQLLSYGVNSNSKNKTLHAEVNLVQRLHRET.......................GRPIPAGAVLYSTHKPCKMCAGMIYHWCEDPSQ...LKVYYSVEEKGGLSRQTVLDQHGLNHHISK C1EBX0_MICSR/256-391 TQLWERDRGVVAALVSPR.GEVTDAARNVNADNKCLHAEWNLLAPTLWGEWVL..SPTEDDEIANRPGAGPEEAGPLEEGTRVLVTLQCCKMCAALVCAAADRPGRRGPIEVVYLNPDDGSLARDTQLRRRGWESRHAA #=GC seq_cons pshacRDRcVsAhLlssp.GtlhssAsNoNucNtsLHAEhNLLhPhhhtp.......................t+sl.sGspLhVTLQCC+MCAAhlsthu-t.ut...hcVsYhpEDsGuLARcTtLcp+GhEp+hst //